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Sodium-transport NADH-quinone reductase of a marineVibrio alginolyticus

Journal of Bioenergetics and Biomembranes volume 21, pages 649–662 (1989)Cite this article

Abstract

The respiratory chain of a marine bacterium,Vibrio alginolyticus, required Na+ for maximum activity, and the site of Na+-dependent activation was localized on the NADH-quinone reductase segment. The Na+-dependent NADH-quinone reductase extruded Na+ as a direct result of redox reaction. It was composed of three subunits, α, β, and γ, with apparentMr of 52, 46, and 32 KDa, respectively. The reduction of ubiquinone-1 to ubiquinol proceeded via ubisemiquinone radicals. The former reaction was catalyzed by the FAD-containing β subunit. This reaction showed no specific requirement for Na+. For the formation of ubiquinol, the presence of the γ subunit and the FMN-containing α subunit was essential. The latter reaction specifically required Na+ for activity and was strongly inhibited by 2-n-heptyl-4-hydroxyquinolineN-oxide. It was assigned to the coupling site for Na+ transport. The mode of energy coupling of redox-driven Na+ pump was compared with those of decarboxylase- and ATP-driven Na+ pumps found in other bacteria.

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  1. Laboratory of Membrane Biochemistry, Faculty of Pharmaceutical Sciences, Chiba University, 1-33, Yayoi-cho, 260, Chiba, Japan

    Tsutomu Unemoto & Maki Hayashi

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  1. Tsutomu Unemoto
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  2. Maki Hayashi
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Unemoto, T., Hayashi, M. Sodium-transport NADH-quinone reductase of a marineVibrio alginolyticus . J Bioenerg Biomembr 21, 649–662 (1989). https://doi.org/10.1007/BF00762684

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  • DOI: https://doi.org/10.1007/BF00762684

Key Words

  • Na+ transport
  • NADH-quinone reductase
  • Na+ pump
  • respiratory chain
  • marine bacteria
  • moderately halophilic bacteria